The molecular mechanism of muscle contraction is a problem that has exercised biophysicists and biochemists for many years. The common view of the mechanism is embodied in the 'cross-bridge hypothesis', in which the relative sliding of thick (myosin) and thin (actin) filaments in cross-striated muscle is brought about by the 'cross-bridges', parts of the myosin molecules which protrude from the thick filaments and interact cyclically with the actin filaments, transporting them by a rowing action that is powered by the hydrolysis of ATP. This hypothesis is, however, rather vague on the molecular details of cross-bridge movement and, in the light of the recently determined crystal structures of myosin and actin, it has evolved into the more precise 'swinging lever-arm hypothesis'. Use of beamline X9B has been essential in collecting data to refine this hypothesis.